English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

1. Glycogen, nucleotides and glycolytic intermediates and products were measured before and during tetanus in the hamstrings-muscle groups of normal (C3H) and phosphorylase kinase-deficient (ICR/IAn) mice. 2. Phosphorylase kinase-deficient muscles contained 3-4-fold more glycogen and sustained a larger (approx. 2-fold), more rapid (11 +/- 2 ng/s faster) and more prolonged glycogenolysis during 120s tetanus despite their lack of phosphorylase a. 3. No significant change in total adenine nucleotide contents occurred during tetanus in either strain, but there was a 60-100-fold rise in IMP concentration to approx. 2mM in both strains. The initial rate of IMP formation was 6-fold more rapid (112 nmol/s per g) in phosphorylase kinase-deficient muscle. 4. Adenylosuccinate content rose to 36 nmol/g in phosphorylase kinase-deficient muscle and to 9 nmol/g in normal muscle at 45s tetanus, but then fell. 5. In phosphorylase kinase-deficient muscle, glucose 6-phosphate, a powerful phosphorylase inhibitor, was 56% of that in normal muscle. 6. The mass-action ratio of the phosphoglucomutase-catalysed reaction [glucose 6-phosphate]/[glucose 1-phosphate] was markedly lower than Keq. (approx. 17) in relaxed muscle of both strains (approx. 5-7), but rose significantly during tetanus to the value for Keq. 7. The data for IMP satisfy the criteria put forward by Rahim, Perrett &amp; Griffiths [(1976) FEBS Lett. 69, 203-206] for a nucleotide activator of phosphorylase b: it should be present at a higher concentration in phosphorylase kinase-deficient muscle, its concentration should rise during muscle work, and it should attain a concentration comparable with its activation constant for phosphorylase b.

Metabolic adaptation in phosphorylase kinase deficiency. Changes in metabolite concentrations during tetanic stimulation of mouse leg muscles